Received 23 October 2013
aDepartment of Chemistry, Howard University, 525 College Street NW, Washington, DC 20059, USA,bDepartment of Chemistry, Catholic University of America, Washington, DC 20064, USA,cNASA Johnson Space Center, Astromaterial and Exploration Science Directorate, Houston, TX 77058, USA, and dSolar System Exploration Division, NASA Goddard Space Flight Center, Greenbelt, MD 20771, USA
Correspondence e-mail: email@example.com
The title compound, C5H11NO2·H2O, is an isomer of the -amino acid valine that crystallizes from water in its zwitterion form as a monohydrate. It is not one of the 20 proteinogenic amino acids that are used in living systems and differs from the natural amino acids in that it has no -H atom. The compound exhibits hydrogen bonding between the water molecule and the carboxylate O atoms and an amine H atom. In addition, there are intermolecular hydrogen-bonding interactions between the carboxylate O atoms and amine H atoms. In the crystal, these extensive N-HO and O-HO hydrogen bonds lead to the formation of a three-dimensional network.
The structure of the title compound or its salts have not been reported to the CCDC but there are reports of homoleptic coordination complexes of zinc(II) with isovaline, see: Strasdelt et al. (2001). For literature related to eighty amino acids that have been detected in meteorites or comets, see: Glavin & Dworkin (2009); Burton et al. (2012). For the role that crystallization plays in chiral separation, see: Blackmond & Klussmann (2007); Blackmond et al. (2008). For the role of the H atom on the -C atom in enhancing the rate of racemization, see: Yamada et al. (1983). For the mechanism of racemization of amino acids lacking an -H atom, see: Pizzarello & Groy (2011). For the role that crystallization can play in the enrichment of L-isovaline, see: Glavin & Dworkin (2009); Bada (2009); Bonner et al. (1979). For normal bond lengths and angles, see: Orpen (1993).
Data collection: CrysAlis PRO (Agilent, 2012); cell refinement: CrysAlis PRO; data reduction: CrysAlis PRO; program(s) used to solve structure: SHELXS97 (Sheldrick, 2008); program(s) used to refine structure: SHELXL97 (Sheldrick, 2008); molecular graphics: SHELXTL (Sheldrick, 2008); software used to prepare material for publication: SHELXTL.
Supplementary data and figures for this paper are available from the IUCr electronic archives (Reference: JJ2178 ).
RJB wishes to acknowledge the NSF-MRI program (grant CHE-0619278) for funds to purchase the diffractometer. GB wishes to acknowledge support of this work from NASA (NNX10AK71A)
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